ID   DSBE_HAEIN              Reviewed;         181 AA.
AC   P45038;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Thiol:disulfide interchange protein DsbE;
DE   AltName: Full=Cytochrome c biogenesis protein CcmG;
GN   Name=dsbE; Synonyms=ccmG; OrderedLocusNames=HI_1095;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Involved in disulfide bond formation. Catalyzes a late,
CC       reductive step in the assembly of periplasmic c-type cytochromes,
CC       probably the reduction of disulfide bonds of the apocytochrome c to
CC       allow covalent linkage with the heme. Possible subunit of a heme lyase
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}; Periplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L42023; AAC22752.1; -; Genomic_DNA.
DR   PIR; B64167; B64167.
DR   RefSeq; NP_439252.1; NC_000907.1.
DR   RefSeq; WP_005657352.1; NC_000907.1.
DR   AlphaFoldDB; P45038; -.
DR   SMR; P45038; -.
DR   STRING; 71421.HI_1095; -.
DR   EnsemblBacteria; AAC22752; AAC22752; HI_1095.
DR   KEGG; hin:HI_1095; -.
DR   PATRIC; fig|71421.8.peg.1140; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_042529_19_1_6; -.
DR   OMA; MIGKPFP; -.
DR   PhylomeDB; P45038; -.
DR   BioCyc; HINF71421:G1GJ1-1130-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR   CDD; cd03010; TlpA_like_DsbE; 1.
DR   InterPro; IPR004799; Periplasmic_diS_OxRdtase_DsbE.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR00385; dsbE; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cytochrome c-type biogenesis;
KW   Disulfide bond; Membrane; Redox-active center; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..181
FT                   /note="Thiol:disulfide interchange protein DsbE"
FT                   /id="PRO_0000201295"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..181
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          38..175
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        78..81
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   181 AA;  20535 MW;  4B334B444179EF24 CRC64;
     MKKKLLVPLI LFLSITIAFL VQLKRNAQGE DIKALESALV GKPVPAKNLT ELFENKTYTN
     ELFQQGEPVL LNVWATWCPT CYAEHQYLNK LAKEGVRIIG LDYKDESPKA MKWLKDLGNP
     YQVVLKDEKG SFGLDLGVYG APETFIVDGK GVIHYRYAGD VNEKVWTQTL KPIYDKLSEQ
     Q